A cell cycle and nutritional checkpoint controlling bacterial surface adhesion.
In natural environments, bacteria often adhere to surfaces where they form complex multicellular communities. Surface adherence is determined by the biochemical composition of the cell envelope. We describe a novel regulatory mechanism by which the bacterium, Caulobacter crescentus, integrates cell...
Main Authors: | , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2014-01-01
|
Series: | PLoS Genetics |
Online Access: | http://europepmc.org/articles/PMC3900383?pdf=render |
id |
doaj-4023feb1191144e280b7664eafc98458 |
---|---|
record_format |
Article |
spelling |
doaj-4023feb1191144e280b7664eafc984582020-11-25T01:16:11ZengPublic Library of Science (PLoS)PLoS Genetics1553-73901553-74042014-01-01101e100410110.1371/journal.pgen.1004101A cell cycle and nutritional checkpoint controlling bacterial surface adhesion.Aretha FiebigJulien HerrouCoralie FumeauxSunish K RadhakrishnanPatrick H ViollierSean CrossonIn natural environments, bacteria often adhere to surfaces where they form complex multicellular communities. Surface adherence is determined by the biochemical composition of the cell envelope. We describe a novel regulatory mechanism by which the bacterium, Caulobacter crescentus, integrates cell cycle and nutritional signals to control development of an adhesive envelope structure known as the holdfast. Specifically, we have discovered a 68-residue protein inhibitor of holdfast development (HfiA) that directly targets a conserved glycolipid glycosyltransferase required for holdfast production (HfsJ). Multiple cell cycle regulators associate with the hfiA and hfsJ promoters and control their expression, temporally constraining holdfast development to the late stages of G1. HfiA further functions as part of a 'nutritional override' system that decouples holdfast development from the cell cycle in response to nutritional cues. This control mechanism can limit surface adhesion in nutritionally sub-optimal environments without affecting cell cycle progression. We conclude that post-translational regulation of cell envelope enzymes by small proteins like HfiA may provide a general means to modulate the surface properties of bacterial cells.http://europepmc.org/articles/PMC3900383?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Aretha Fiebig Julien Herrou Coralie Fumeaux Sunish K Radhakrishnan Patrick H Viollier Sean Crosson |
spellingShingle |
Aretha Fiebig Julien Herrou Coralie Fumeaux Sunish K Radhakrishnan Patrick H Viollier Sean Crosson A cell cycle and nutritional checkpoint controlling bacterial surface adhesion. PLoS Genetics |
author_facet |
Aretha Fiebig Julien Herrou Coralie Fumeaux Sunish K Radhakrishnan Patrick H Viollier Sean Crosson |
author_sort |
Aretha Fiebig |
title |
A cell cycle and nutritional checkpoint controlling bacterial surface adhesion. |
title_short |
A cell cycle and nutritional checkpoint controlling bacterial surface adhesion. |
title_full |
A cell cycle and nutritional checkpoint controlling bacterial surface adhesion. |
title_fullStr |
A cell cycle and nutritional checkpoint controlling bacterial surface adhesion. |
title_full_unstemmed |
A cell cycle and nutritional checkpoint controlling bacterial surface adhesion. |
title_sort |
cell cycle and nutritional checkpoint controlling bacterial surface adhesion. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS Genetics |
issn |
1553-7390 1553-7404 |
publishDate |
2014-01-01 |
description |
In natural environments, bacteria often adhere to surfaces where they form complex multicellular communities. Surface adherence is determined by the biochemical composition of the cell envelope. We describe a novel regulatory mechanism by which the bacterium, Caulobacter crescentus, integrates cell cycle and nutritional signals to control development of an adhesive envelope structure known as the holdfast. Specifically, we have discovered a 68-residue protein inhibitor of holdfast development (HfiA) that directly targets a conserved glycolipid glycosyltransferase required for holdfast production (HfsJ). Multiple cell cycle regulators associate with the hfiA and hfsJ promoters and control their expression, temporally constraining holdfast development to the late stages of G1. HfiA further functions as part of a 'nutritional override' system that decouples holdfast development from the cell cycle in response to nutritional cues. This control mechanism can limit surface adhesion in nutritionally sub-optimal environments without affecting cell cycle progression. We conclude that post-translational regulation of cell envelope enzymes by small proteins like HfiA may provide a general means to modulate the surface properties of bacterial cells. |
url |
http://europepmc.org/articles/PMC3900383?pdf=render |
work_keys_str_mv |
AT arethafiebig acellcycleandnutritionalcheckpointcontrollingbacterialsurfaceadhesion AT julienherrou acellcycleandnutritionalcheckpointcontrollingbacterialsurfaceadhesion AT coraliefumeaux acellcycleandnutritionalcheckpointcontrollingbacterialsurfaceadhesion AT sunishkradhakrishnan acellcycleandnutritionalcheckpointcontrollingbacterialsurfaceadhesion AT patrickhviollier acellcycleandnutritionalcheckpointcontrollingbacterialsurfaceadhesion AT seancrosson acellcycleandnutritionalcheckpointcontrollingbacterialsurfaceadhesion AT arethafiebig cellcycleandnutritionalcheckpointcontrollingbacterialsurfaceadhesion AT julienherrou cellcycleandnutritionalcheckpointcontrollingbacterialsurfaceadhesion AT coraliefumeaux cellcycleandnutritionalcheckpointcontrollingbacterialsurfaceadhesion AT sunishkradhakrishnan cellcycleandnutritionalcheckpointcontrollingbacterialsurfaceadhesion AT patrickhviollier cellcycleandnutritionalcheckpointcontrollingbacterialsurfaceadhesion AT seancrosson cellcycleandnutritionalcheckpointcontrollingbacterialsurfaceadhesion |
_version_ |
1725150734194835456 |